ID A0A2S5KHX3_9PROT Unreviewed; 826 AA.
AC A0A2S5KHX3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=C4K68_26105 {ECO:0000313|EMBL:PPC74411.1};
OS Proteobacteria bacterium 228.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=2083153 {ECO:0000313|EMBL:PPC74411.1, ECO:0000313|Proteomes:UP000238196};
RN [1] {ECO:0000313|EMBL:PPC74411.1, ECO:0000313|Proteomes:UP000238196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=228 {ECO:0000313|EMBL:PPC74411.1,
RC ECO:0000313|Proteomes:UP000238196};
RA Krishnan R., Ramesh Kumar N.;
RT "novel marine gammaproteobacteria from coastal saline agro ecosystem.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPC74411.1}.
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DR EMBL; PRLP01000148; PPC74411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5KHX3; -.
DR OrthoDB; 5287177at2; -.
DR Proteomes; UP000238196; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR013668; RNase_R_HTH_12.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08461; HTH_12; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 2.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW Reference proteome {ECO:0000313|Proteomes:UP000238196};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 652..733
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 743..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..826
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 92738 MW; 68D4D6BF2A89F682 CRC64;
MSDHNPPLND DPFAQREAEK YDNPVPSREF LLEYLQNFAG PATHEQLCEA LELHDEERIE
ALRRRLRAME RDGQLIFTRK GGYGLVNKMD LIAGRVMGHR DGFGFVVPDD GSDDLYLHER
QMRAVFDGDR VLVRVRGEDF KGRREAAIVE VVERAVSRLV GRYFEEYGNA FVTPDNTKIA
QDVLIRADGS VRARQGQVVL VEIDEYPSKR GHAVGRIVQI LGDHLAPGME TQVAIYNYGI
PNEWSDEALA ELDAIAEEVA ESDKQGRVDL RHLPLVTIDG EDARDFDDAV YAERKKGGGW
RLYVAIADVS HYIRPGTALD QEALKRGNST YFPGQVVPML PEKISNGLCS LNPQVDRLAM
VCETTISAAG NISGYKFYEA VFQSQARLTY TKVSQMLERP DSSDGQELRQ RYTALVPHLE
ALFELYHALR VARDVRGAID FETTETRIVF GEGRKIDQVV PVQRNEAHRL IEECMLCANV
CAARFLQKNK LPALYRIHEG PKAERLDKLR AYLAPLGLNL SGGDKPQPSD YQALLSSIQQ
RPDYHPIQTM LLRSMSQAVY SPDNEGHFGL GYKAYTHFTS PIRRYPDLLV HRAIRALLRR
EQSEGALYGY HYDLQAMVAL GEQCSSTERR SDEASRDVVS WLKCEYMSHR VGEEYQGVIS
AVTNFGCFIE LSEVYVEGLV HVSGLPGDYY HYDAAFQRLK GERTGKSFRL GDQVRVRVSR
VDLDERKIDF ELIEGPARRV SKSVRDRLRD GDIPPAPART ASQEKVGTTG AKSGGKGAGS
RKPKGSSTAS AGKEKKARKA KVKASIKAKR KAKETSRANK KHAQPH
//
